Misfolded plant virus proteins: elicitors and targets of ubiquitylation

Jockusch, Harald; Wiegand, Christiane

doi:10.1016/s0014-5793(03)00549-0

Cited by 18 publications

(13 citation statements)

References 21 publications

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“…As the error rate of viral polymerases generates mutations at high frequency, it is not unexpected that misfolded and insoluble viral structural proteins are produced during viral multiplication. It was shown for TMV that such proteins are massively polyubiquitinated (Jockusch and Wiegand, 2003). As functional proteins are not targeted, these ubiquitination events are likely to correspond to a cellular protein response to stress (Sugio et al, 2009) rather than a specific regulatory process.…”

Section: Polyubiquitination and Degradation Of Viral Structural Proteinsmentioning

confidence: 99%

Ubiquitin and Plant Viruses, Let’s Play Together!

2012

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Section: Polyubiquitination and Degradation Of Viral Structural Proteinsmentioning

confidence: 99%

Ubiquitin and Plant Viruses, Let’s Play Together!

2012

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“…The CPR is induced by the accumulation of unstable or misfolded proteins in the cytosol and is associated with the induction of a specific subset of HSP70 genes. For example, virus infection in the cytosol in plant or animal cells triggers the induction of HSPs (Whitham et al, 2003), a process that is exacerbated when the virus-encoded proteins are unstable (Jockusch et al, 2001;Jockusch and Wiegand, 2003). The Arabidopsis genome encodes five soluble cytosolic HSP70s, HSP70 (referred to as HSP70A in this article) and HSP70B, and three constitutively expressed HSPs, HSC70-1, HSC70-2, and HSC70-3.…”

Section: Introductionmentioning

confidence: 99%

The Cytosolic Protein Response as a Subcomponent of the Wider Heat Shock Response inArabidopsis

et al. 2009

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In common with a range of environmental and biological stresses, heat shock results in the accumulation of misfolded proteins and a collection of downstream consequences for cellular homeostasis and growth. Within this complex array of responses, the sensing of and responses to misfolded proteins in specific subcellular compartments involves specific chaperones, transcriptional regulators, and expression profiles. Using biological (ectopic protein expression and virus infection) and chemical triggers for misfolded protein accumulation, we have profiled the transcriptional features of the response to misfolded protein accumulation in the cytosol (i.e., the cytoplasmic protein response [CPR]) and identified the effects as a subcomponent of the wider effects induced by heat shock. The CPR in Arabidopsis thaliana is associated with the heat shock promoter element and the involvement of specific heat shock factors (HSFs), notably HSFA2, which appears to be regulated by alternative splicing and non-sense-mediated decay. Characterization of Arabidopsis HSFA2 knockout and overexpression lines showed that HSFA2 is one of the regulatory components of the CPR.

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“…In addition, the proteasome can interfere with the translation of viral RNA and mRNA in virus-infected cells (3,5,8,14,16,22). Ballut et al.…”

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confidence: 99%